Výsledky vyhledávání - "J D, Satterlee"

Detailed NMR analysis of the heme-protein interactions in component IV Glycera dibranchiata monomeric hemoglobin-CO

Autor: S L, Alam, B F, Volkman, J L, Markley, J D, Satterlee

Publikováno v: Journal of biomolecular NMR. 11(2)

Complete 13C, 15N, and 1H resonance assignments have been obtained for the recombinant, ferrous CO-ligated from of component IV monomeric hemoglobin from Glycera dibranchiata. This 15642 Da myoglobin-like protein contains a large number of glycine an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::930ba2dcf5773eee420bc41b31b2d9e4
https://pubmed.ncbi.nlm.nih.gov/9679291

Zobrazit plný text záznamu

Proton NMR comparison of the Saccharomyces cerevisiae ferricytochrome c isozyme-1 monomer and covalent disulfide dimer

Autor: S J Moench, J D Satterlee

Publikováno v: Journal of Biological Chemistry. 264:9923-9931

Proton NMR studies of Saccharomyces cerevisiae (bakers yeast) isozyme-1 monomer and dimer ferricytochrome c have been carried out. The dimer is formed via a disulfide bridge between the Cys-102 residues of monomer proteins. Nuclear Overhauser effect

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::98413f3da45e1630243b351c4d7b5a0d
https://doi.org/10.1016/s0021-9258(18)81748-3

Zobrazit plný text záznamu

Mechanism of T1 relaxation in 13CO complexed to an iron porphyrin: implications for CO bonding in heme proteins

Autor: J. D. Satterlee, T. Perkins, J. H. Richards

Publikováno v: Journal of the American Chemical Society. 105:1350-1354

Chemical shifts and spin-lattice relaxation parameters for ^(13)CO bonded to the complex 1 -methylimidazole-iron protoporphyrin dimethyl ester are reported. The ^(13)CO chemical shifts are much different from those observed in the carbonyl vertebrate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ba0edbea0bf661b99fa083a6c0608442
https://doi.org/10.1021/ja00343a047

Zobrazit plný text záznamu

Aggregation of uroporphyrin I and its metal derivatives in aqueous solution: Raman difference spectroscopy and absorption spectroscopy

Autor: J. D. Satterlee, M. M. Dobry, John A. Shelnutt

Publikováno v: The Journal of Physical Chemistry. 88:4980-4987

Absorption and resonance Raman difference spectra of uroporphyrin I and several of its metal derivatives are given for monomeric and aggregated forms in aqueous solution. These spectral changes are examined in detail herein. An equilibrium model of t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cf7a08c0539eb77afe9d8ebecfeedae9
https://doi.org/10.1021/j150665a038

Zobrazit plný text záznamu

Temperature and pH dependence of the proton magnetic hyperfine resonances of cytochrome c peroxidase-cyanide. Evidence for hindered vinyl group rotation as a mediator of the enzymes activity

Autor: J D Satterlee, J E Erman

Publikováno v: Journal of Biological Chemistry. 258:1050-1056

Proton nmr studies of the hyperfine resonances of cytochrome c peroxidase reveal that two pH-dependent processes can be monitored. One of these is the simple pH titration of a resonance which has been previously assigned to the alpha-vinyl proton at

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d6cd2b6a7e307f72b5148105dad61cca
https://doi.org/10.1016/s0021-9258(18)33157-0

Zobrazit plný text záznamu

Evaluation of the extent of heterogeneity in the Glycera dibranchiata monomer haemoglobin fraction by the use of n.m.r. and ion-exchange chromatography

Autor: I Constantinidis, J D Satterlee, R L Kandler

Publikováno v: Biochemical Journal. 226:131-138

The coelomic haemoglobin of Glycera dibranchiata is known to be separable into monomeric and higher-Mr fractions. Although exhibiting homogeneity with respect to Mr, the extent of haemoglobin heterogeneity for the monomer fraction has never been adeq

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1754cb2e980df4ede4b375801d0f6c1
https://doi.org/10.1042/bj2260131

Zobrazit plný text záznamu

Proton hyperfine resonance assignments in cyanide-ligated cytochrome c peroxidase using the nuclear Overhauser effect

Autor: J D Satterlee, J E Erman, J S DeRopp

Publikováno v: Journal of Biological Chemistry. 262:11578-11583

The development of the proton nuclear Overhauser effect (NOE) for hyperfine shifted resonances of cyanide-ligated cytochrome c peroxidase (Saccharomyces cerevisiae) has been studied. In the pre-steady state regime, the major effects are due to primar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9776bc2d62fcb896ae53ba27a2868fca
https://doi.org/10.1016/s0021-9258(18)60847-6

Zobrazit plný text záznamu

Proton nuclear magnetic resonance characterization of the oxidized intermediates of cytochrome c peroxidase

Autor: J E Erman, J D Satterlee

Publikováno v: Journal of Biological Chemistry. 256:1091-1093

Oxidation of cytochrome c peroxidase with hydrogen peroxide to form the initial oxidized intermediate, cytochrome c peroxidase compound I, drastically alters the proton hyperfine nmr spectrum. In contrast to studies of horseradish peroxidase, where t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f2cbb14dfc03dcce95f8c05b49593ed7
https://doi.org/10.1016/s0021-9258(19)69928-x

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání